SUBI_ECOLI
ID SUBI_ECOLI Reviewed; 329 AA.
AC P0AG78; P06997; Q2M8L3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Sulfate-binding protein;
DE AltName: Full=Sulfate starvation-induced protein 2;
DE Short=SSI2;
DE Flags: Precursor;
GN Name=sbp; OrderedLocusNames=b3917, JW3888;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3158524; DOI=10.1111/j.1432-1033.1985.tb08934.x;
RA Hellinga H.W., Evans P.R.;
RT "Nucleotide sequence and high-level expression of the major Escherichia
RT coli phosphofructokinase.";
RL Eur. J. Biochem. 149:363-373(1985).
RN [2]
RP SEQUENCE REVISION.
RA Evans P.R.;
RL Submitted (OCT-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 152-164; 176-178 AND 201-203, AND MUTAGENESIS.
RX PubMed=2002055; DOI=10.1016/s0021-9258(19)67775-6;
RA Jacobson B.L., He J.J., Vermersch P.S., Lemon D.D., Quiocho F.A.;
RT "Engineered interdomain disulfide in the periplasmic receptor for sulfate
RT transport reduces flexibility. Site-directed mutagenesis and ligand-binding
RT studies.";
RL J. Biol. Chem. 266:5220-5225(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 20-31.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 20-29; 42-48; 256-263; 265-273 AND 277-282.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
CC -!- FUNCTION: This protein specifically binds sulfate and is involved in
CC its transmembrane transport.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Repressed by sulfate or cysteine.
CC -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC {ECO:0000305}.
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DR EMBL; X02519; CAA26357.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L19201; AAB03049.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76899.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77393.1; -; Genomic_DNA.
DR PIR; S40860; BYEC.
DR RefSeq; NP_418352.1; NC_000913.3.
DR RefSeq; WP_001045689.1; NZ_SSUV01000029.1.
DR AlphaFoldDB; P0AG78; -.
DR SMR; P0AG78; -.
DR BioGRID; 4261220; 30.
DR ComplexPortal; CPX-4386; Sulfate/thiosulfate ABC transporter complex, sbp variant.
DR DIP; DIP-35843N; -.
DR IntAct; P0AG78; 11.
DR STRING; 511145.b3917; -.
DR TCDB; 3.A.1.6.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AG78; -.
DR PaxDb; P0AG78; -.
DR PRIDE; P0AG78; -.
DR EnsemblBacteria; AAC76899; AAC76899; b3917.
DR EnsemblBacteria; BAE77393; BAE77393; BAE77393.
DR GeneID; 66672175; -.
DR GeneID; 948411; -.
DR KEGG; ecj:JW3888; -.
DR KEGG; eco:b3917; -.
DR PATRIC; fig|1411691.4.peg.2788; -.
DR EchoBASE; EB0922; -.
DR eggNOG; COG1613; Bacteria.
DR HOGENOM; CLU_055615_0_1_6; -.
DR InParanoid; P0AG78; -.
DR OMA; KDFGGWK; -.
DR PhylomeDB; P0AG78; -.
DR BioCyc; EcoCyc:SBP-MON; -.
DR BioCyc; MetaCyc:SBP-MON; -.
DR PRO; PR:P0AG78; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0035796; C:ATP-binding cassette (ABC) transporter complex, transmembrane substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0043199; F:sulfate binding; IDA:EcoCyc.
DR GO; GO:1902358; P:sulfate transmembrane transport; IC:ComplexPortal.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc.
DR GO; GO:0015709; P:thiosulfate transport; IC:ComplexPortal.
DR CDD; cd01005; PBP2_CysP; 1.
DR InterPro; IPR000957; Sulphate/thiosulphate-bd_CS.
DR InterPro; IPR034408; Sulphate/thiosulphate_BS.
DR InterPro; IPR005669; Thiosulph/SO4-bd.
DR PANTHER; PTHR30368; PTHR30368; 1.
DR TIGRFAMs; TIGR00971; 3a0106s03; 1.
DR PROSITE; PS00401; PROK_SULFATE_BIND_1; 1.
DR PROSITE; PS00757; PROK_SULFATE_BIND_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Periplasm; Reference proteome; Signal;
KW Sulfate transport; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8774726,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 20..329
FT /note="Sulfate-binding protein"
FT /id="PRO_0000031683"
FT CONFLICT 185
FT /note="V -> E (in Ref. 1; CAA26357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 36659 MW; 3353D36DE484C814 CRC64;
MNKWGVGLTF LLAATSVMAK DIQLLNVSYD PTRELYEQYN KAFSAHWKQQ TGDNVVIRQS
HGGSGKQATS VINGIEADVV TLALAYDVDA IAERGRIDKE WIKRLPDNSA PYTSTIVFLV
RKGNPKQIHD WNDLIKPGVS VITPNPKSSG GARWNYLAAW GYALHHNNND QAKAQDFVRA
LYKNVEVLDS GARGSTNTFV ERGIGDVLIA WENEALLAAN ELGKDKFEIV TPSESILAEP
TVSVVDKVVE KKGTKEVAEA YLKYLYSPEG QEIAAKNYYR PRDAEVAKKY ENAFPKLKLF
TIDEEFGGWT KAQKEHFANG GTFDQISKR
